Isolation and characterization of synergistic hemorrhagins from the venom of the snake Bothrops asper
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| Autores: | , , |
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| Formato: | artículo original |
| Fecha de Publicación: | 1993 |
| Descripción: | Three hemorrhagic factors (BaH1, BH2 and BH3) were isolated from the venom of Bothrops asper by gel filtration on Sephacryl S-200, DEAE-Sepharose chromatography, metal chelate affinity chromatography and hydrophobic interaction chromatography. They contain 55% of the total hemorrhagic activity of the whole venom when they are mixed, but lose almost half of the activity if they are separated, indicating a synergism between the three. The main hemorrhagin is BaH1 (Bothrops asper hemorrhagin 1); the other two are weak hemorrhagins but contribute to the synergism. They are acidic proteins with a pI of 4.5, 5.2 and 5; their mol. wt is 64,000, 26,000 and 55,000 respectively. The minimal hemorrhagic dose (MHD) of BaH1, BH2 and BH3 is 0.18, 2 and 1.6 micrograms, with a specific activity 55, 5 and 6.25 higher than that of the whole venom. The hemorrhagic activity of all three factors was inhibited by EDTA and ortho-phenathroline, indicating that the hemorrhagic activity is metal dependent. Phosphoramidon, soybean trypsin inhibitor, PMSF, pepstatin and aprotinin did not affect the hemorrhagic activity of the isolated factors. |
| País: | Kérwá |
| Institución: | Universidad de Costa Rica |
| Repositorio: | Kérwá |
| OAI Identifier: | oai:https://www.kerwa.ucr.ac.cr:10669/29227 |
| Acceso en línea: | https://hdl.handle.net/10669/29227 |
| Access Level: | acceso abierto |
| Palabra clave: | Aminosalicylic Acid Ammonium Sulfate Animals Antibody Specificity Antivenins Chromatography, Gel Chromatography, Ion Exchange Cross Reactions Crotalid Venoms Drug Synergism Endopeptidases Enzyme Inhibitors Hemorrhage Hydrogen-Ion Concentration Immunodiffusion Immunoelectrophoresis Isoelectric Focusing Mice Molecular Weight |